Molecular basis for the recognition of the substrate and for the transglycosylation reaction of an exo-type alpha-amylase.
| Project/Area Number |
26450100
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Multi-year Fund |
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| Section | 一般 |
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| Research Field |
Applied microbiology
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| Research Institution | Osaka Prefecture University |
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Principal Investigator |
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| Co-Investigator(Kenkyū-buntansha) |
西村 重徳 大阪府立大学, 生命環境科学研究科, 助教 (90244665)
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| Project Period (FY) |
2014-04-01 – 2017-03-31
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| Project Status |
Completed (Fiscal Year 2016)
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| Budget Amount *help |
¥5,070,000 (Direct Cost: ¥3,900,000、Indirect Cost: ¥1,170,000)
Fiscal Year 2016: ¥1,430,000 (Direct Cost: ¥1,100,000、Indirect Cost: ¥330,000)
Fiscal Year 2015: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2014: ¥2,080,000 (Direct Cost: ¥1,600,000、Indirect Cost: ¥480,000)
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| Keywords | glycosides / maltotriose / amylase / transglycosylation / アミラーゼ / マルトトリオース生成アミラーゼ / 糖転移反応 / 配糖体 / マルトトリオース |
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| Outline of Final Research Achievements |
Glycosidation is one of the important modification methods for useful compounds, and is known as a modifier of the solubility, stability, absorbability, and taste quality. In this study, we aimed to approach the molecular mechanism for transglycosylation reaction and to obtain the mutant enzymes having effective activity for transglycosylation, based on the structural information of a maltotriose-forming amylase. As a result, we succeed the identification of the amino acids involving maltotriose-specific cleavage and the acquisition of the mutant enzymes with extreme high transglycosylation activity.
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Report
(4 results)
Research Products
(8 results)
